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P26883

- FKB1A_MOUSE

UniProt

P26883 - FKB1A_MOUSE

Protein

Peptidyl-prolyl cis-trans isomerase FKBP1A

Gene

Fkbp1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.By similarity

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    Enzyme regulationi

    Inhibited by both FK506 and rapamycin.

    GO - Molecular functioni

    1. calcium channel inhibitor activity Source: RefGenome
    2. drug binding Source: MGI
    3. FK506 binding Source: MGI
    4. ion channel binding Source: BHF-UCL
    5. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome
    6. protein binding Source: MGI
    7. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. chaperone-mediated protein folding Source: RefGenome
    2. cytokine-mediated signaling pathway Source: MGI
    3. heart morphogenesis Source: BHF-UCL
    4. heart trabecula formation Source: BHF-UCL
    5. muscle contraction Source: MGI
    6. negative regulation of protein phosphorylation Source: MGI
    7. negative regulation of release of sequestered calcium ion into cytosol Source: RefGenome
    8. protein peptidyl-prolyl isomerization Source: RefGenome
    9. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    10. release of sequestered calcium ion into cytosol Source: MGI
    11. response to caffeine Source: MGI
    12. response to iron ion Source: Ensembl
    13. T cell proliferation Source: MGI
    14. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    ReactomeiREACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_224217. TGFBR1 LBD Mutants in Cancer.
    REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_224802. TGFBR1 KD Mutants in Cancer.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP1A (EC:5.2.1.8)
    Short name:
    PPIase FKBP1A
    Alternative name(s):
    12 kDa FK506-binding protein
    Short name:
    12 kDa FKBP
    Short name:
    FKBP-12
    Calstabin-1
    FK506-binding protein 1A
    Short name:
    FKBP-1A
    Immunophilin FKBP12
    Rotamase
    Gene namesi
    Name:Fkbp1a
    Synonyms:Fkbp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:95541. Fkbp1a.

    Subcellular locationi

    GO - Cellular componenti

    1. axon terminus Source: Ensembl
    2. membrane Source: MGI
    3. sarcoplasmic reticulum membrane Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1APRO_0000075290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycineBy similarity
    Modified residuei9 – 91PhosphoserineBy similarity
    Modified residuei53 – 531N6-acetyllysine; alternate1 Publication
    Modified residuei53 – 531N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26883.
    PaxDbiP26883.
    PRIDEiP26883.

    PTM databases

    PhosphoSiteiP26883.

    Expressioni

    Gene expression databases

    ArrayExpressiP26883.
    BgeeiP26883.
    CleanExiMM_FKBP1A.
    GenevestigatoriP26883.

    Interactioni

    Subunit structurei

    Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation By similarity. Interacts with ACVR1B and SMAD7. Interacts directly with RYR1, RYR2 and RYR3 By similarity. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1).By similarity1 Publication

    Protein-protein interaction databases

    BioGridi199682. 3 interactions.
    DIPiDIP-29707N.
    IntActiP26883. 3 interactions.
    MINTiMINT-4095099.

    Structurei

    3D structure databases

    ProteinModelPortaliP26883.
    SMRiP26883. Positions 2-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10889PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0545.
    GeneTreeiENSGT00550000074272.
    HOGENOMiHOG000154887.
    HOVERGENiHBG051623.
    KOiK09568.
    OMAiSPQKGDT.
    OrthoDBiEOG7ZGX5T.
    TreeFamiTF105291.

    Family and domain databases

    InterProiIPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 1 hit.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P26883-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT    50
    LGKQEVIRGW EEGVAQMSVG QRAKLIISSD YAYGATGHPG IIPPHATLVF 100
    DVELLKLE 108
    Length:108
    Mass (Da):11,923
    Last modified:January 23, 2007 - v2
    Checksum:i8C265ED5803F6987
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60203 mRNA. Translation: CAA42762.1.
    U65100, U65098, U65099 Genomic DNA. Translation: AAB17554.1.
    AF483488 mRNA. Translation: AAL90762.1.
    AF483489 mRNA. Translation: AAL90763.1.
    AK002777 mRNA. Translation: BAB22351.1.
    AK010693 mRNA. Translation: BAB27125.1.
    AK019362 mRNA. Translation: BAB31680.1.
    AK154751 mRNA. Translation: BAE32804.1.
    AK168333 mRNA. Translation: BAE40271.1.
    AK169186 mRNA. Translation: BAE40963.1.
    AK169242 mRNA. Translation: BAE41008.1.
    BC004671 mRNA. Translation: AAH04671.1.
    CCDSiCCDS16869.1.
    PIRiJH0528.
    RefSeqiNP_032045.1. NM_008019.2.
    XP_006498811.1. XM_006498748.1.
    UniGeneiMm.278458.
    Mm.487732.

    Genome annotation databases

    EnsembliENSMUST00000044011; ENSMUSP00000037206; ENSMUSG00000032966.
    GeneIDi14225.
    KEGGimmu:14225.
    UCSCiuc008ndy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60203 mRNA. Translation: CAA42762.1 .
    U65100 , U65098 , U65099 Genomic DNA. Translation: AAB17554.1 .
    AF483488 mRNA. Translation: AAL90762.1 .
    AF483489 mRNA. Translation: AAL90763.1 .
    AK002777 mRNA. Translation: BAB22351.1 .
    AK010693 mRNA. Translation: BAB27125.1 .
    AK019362 mRNA. Translation: BAB31680.1 .
    AK154751 mRNA. Translation: BAE32804.1 .
    AK168333 mRNA. Translation: BAE40271.1 .
    AK169186 mRNA. Translation: BAE40963.1 .
    AK169242 mRNA. Translation: BAE41008.1 .
    BC004671 mRNA. Translation: AAH04671.1 .
    CCDSi CCDS16869.1.
    PIRi JH0528.
    RefSeqi NP_032045.1. NM_008019.2.
    XP_006498811.1. XM_006498748.1.
    UniGenei Mm.278458.
    Mm.487732.

    3D structure databases

    ProteinModelPortali P26883.
    SMRi P26883. Positions 2-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199682. 3 interactions.
    DIPi DIP-29707N.
    IntActi P26883. 3 interactions.
    MINTi MINT-4095099.

    PTM databases

    PhosphoSitei P26883.

    Proteomic databases

    MaxQBi P26883.
    PaxDbi P26883.
    PRIDEi P26883.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044011 ; ENSMUSP00000037206 ; ENSMUSG00000032966 .
    GeneIDi 14225.
    KEGGi mmu:14225.
    UCSCi uc008ndy.1. mouse.

    Organism-specific databases

    CTDi 2280.
    MGIi MGI:95541. Fkbp1a.

    Phylogenomic databases

    eggNOGi COG0545.
    GeneTreei ENSGT00550000074272.
    HOGENOMi HOG000154887.
    HOVERGENi HBG051623.
    KOi K09568.
    OMAi SPQKGDT.
    OrthoDBi EOG7ZGX5T.
    TreeFami TF105291.

    Enzyme and pathway databases

    Reactomei REACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_224217. TGFBR1 LBD Mutants in Cancer.
    REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_224802. TGFBR1 KD Mutants in Cancer.

    Miscellaneous databases

    NextBioi 285479.
    PROi P26883.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26883.
    Bgeei P26883.
    CleanExi MM_FKBP1A.
    Genevestigatori P26883.

    Family and domain databases

    InterProi IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 1 hit.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA encoding murine FK506-binding protein (FKBP): nucleotide and deduced amino acid sequence."
      Nelson P.A., Lippke J.A., Murcko M.A., Rosborough S.L., Peattie D.A.
      Gene 109:255-258(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X CBA.
    2. Shou W., Bao S., Mathews L.S., Matzuk M.M.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: 129/Sv.
    3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: ILS and ISS.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Hippocampus.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    6. "Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
      Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
      Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; RYR1 AND PROTEIN PHOSPHATASE 1.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiFKB1A_MOUSE
    AccessioniPrimary (citable) accession number: P26883
    Secondary accession number(s): Q545E9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3